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Article

A lysine-to-arginine change found in natural alleles of the human T-cell lymphotropic/leukemia virus type 1 p12(I) protein greatly influences its stability.

Journal of virology - 1 Aug 1999

Trovato R, Mulloy J C, Johnson J M, Takemoto S, de Oliveira M P, Franchini G

Abstract excerpt

The HTLV-1 singly spliced open reading frame I protein, p12(I), is highly unstable and appears to be necessary for persistent infection in rabbits. Here we demonstrate that p12(I) forms dimers through two putative leucine zipper domains and that its stability is augmented by specific proteasome inhibitors. p12(I) is ubiquitylated, and mutations of its unique carboxy-terminus lysine residue to an arginine greatly...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Share to Leukemia-Lymphoma, Adult T-Cell

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Source

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Identifiers

PMID: 10400740
DOI: 10.1128/JVI.73.8.6460-6467.1999
PMCID: PMC112727

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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